ID A0A0N8W8J2_9EURY Unreviewed; 411 AA.
AC A0A0N8W8J2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Translation initiation factor 2 subunit gamma {ECO:0000256|HAMAP-Rule:MF_00119};
DE EC=3.6.5.3 {ECO:0000256|HAMAP-Rule:MF_00119};
DE AltName: Full=aIF2-gamma {ECO:0000256|HAMAP-Rule:MF_00119};
DE AltName: Full=eIF-2-gamma {ECO:0000256|HAMAP-Rule:MF_00119};
GN Name=eif2g {ECO:0000256|HAMAP-Rule:MF_00119};
GN ORFNames=APR55_10505 {ECO:0000313|EMBL:KQC09251.1};
OS Methanolinea sp. SDB.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanolinea.
OX NCBI_TaxID=1735327 {ECO:0000313|EMBL:KQC09251.1, ECO:0000313|Proteomes:UP000050878};
RN [1] {ECO:0000313|EMBL:KQC09251.1, ECO:0000313|Proteomes:UP000050878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC09251.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA.
CC {ECO:0000256|HAMAP-Rule:MF_00119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001874, ECO:0000256|HAMAP-
CC Rule:MF_00119};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00119};
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000256|HAMAP-Rule:MF_00119}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQC09251.1}.
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DR EMBL; LKUF01000163; KQC09251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8W8J2; -.
DR Proteomes; UP000050878; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00119; eIF_2_gamma; 1.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR022424; TIF2_gsu.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR NCBIfam; TIGR03680; eif2g_arch; 1.
DR PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00119};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00119};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00119}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00119};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00119};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00119};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00119}; Zinc {ECO:0000256|HAMAP-Rule:MF_00119}.
FT DOMAIN 6..203
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 18..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
FT BINDING 181..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00119"
SQ SEQUENCE 411 AA; 44505 MW; FFA46AF4528B6884 CRC64;
MRDVTIPSVN IGVVGHVDHG KTTLVYDLTN AWTDRHSEEI KRGISIRLGY ADATFYRCDK
CEGQDAYSSK PECPVCGGKA EPFRSVSFVD APGHETLMAT MLSGSALMDG AMLVIAANEP
CPQPQTKEHL MALELVGISR IVIVQNKIDV VPQKEALRHY EQIKKFVKGT IAENAPIIPV
SAQKDINVGA LIEALNETIP DVERDPGADP LMLVARSFDI NKPGSSWRDV KGGVIGGSLI
RGVLKESDDI EIRPGRQVQV ENRIRWEPIT TRITTINAGS RKVTEATPGG LLGLGTKLDP
ALTKSDALAG QVVGHVGKLP PVRDRLKFRV TLMERVVGSS SELVIEPLKH NEPLMLSVGT
AVTVGVVSST KKDLSEVVLK RPVCVEVGAR IAISRQLGAR WRLIGMGELT E
//
